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Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide

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Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide. / Grahl, Sabine; Maillard, Julien; Spronk, Chris A. E. M.; Vuister, Geerten W.; Sargent, Frank (Lead / Corresponding author).

In: Molecular Microbiology, Vol. 83, No. 6, 03.2012, p. 1254-1267.

Research output: Contribution to journalArticle

Harvard

Grahl, S, Maillard, J, Spronk, CAEM, Vuister, GW & Sargent, F 2012, 'Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide' Molecular Microbiology, vol 83, no. 6, pp. 1254-1267.

APA

Grahl, S., Maillard, J., Spronk, C. A. E. M., Vuister, G. W., & Sargent, F. (2012). Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide. Molecular Microbiology, 83(6), 1254-1267doi: 10.1111/j.1365-2958.2012.08005.x

Vancouver

Grahl S, Maillard J, Spronk CAEM, Vuister GW, Sargent F. Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide. Molecular Microbiology. 2012 Mar;83(6):1254-1267.

Author

Grahl, Sabine; Maillard, Julien; Spronk, Chris A. E. M.; Vuister, Geerten W.; Sargent, Frank (Lead / Corresponding author) / Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide.

In: Molecular Microbiology, Vol. 83, No. 6, 03.2012, p. 1254-1267.

Research output: Contribution to journalArticle

Bibtex - Download

@article{0ab9262ab8ca41b0ac9a038e7aa412e9,
title = "Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide",
author = "Sabine Grahl and Julien Maillard and Spronk, {Chris A. E. M.} and Vuister, {Geerten W.} and Frank Sargent",
year = "2012",
volume = "83",
number = "6",
pages = "1254--1267",
journal = "Molecular Microbiology",
issn = "0950-382X",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Overlapping transport and chaperone-binding functions within a bacterial twin-arginine signal peptide

A1 - Grahl,Sabine

A1 - Maillard,Julien

A1 - Spronk,Chris A. E. M.

A1 - Vuister,Geerten W.

A1 - Sargent,Frank

AU - Grahl,Sabine

AU - Maillard,Julien

AU - Spronk,Chris A. E. M.

AU - Vuister,Geerten W.

AU - Sargent,Frank

PY - 2012/3

Y1 - 2012/3

N2 - <p>The twin-arginine translocation (Tat) pathway is a protein targeting system present in many prokaryotes. The physiological role of the Tat pathway is the transmembrane translocation of fully-folded proteins, which are targeted by N-terminal signal peptides bearing conserved SRRxFLK twin-arginine amino acid motifs. In Escherichia coli the majority of Tat targeted proteins bind redox cofactors and it is important that only mature, cofactor-loaded precursors are presented for export. Cellular processes have been unearthed that sequence these events, for example the signal peptide of the periplasmic nitrate reductase (NapA) is bound by a cytoplasmic chaperone (NapD) that is thought to regulate assembly and export of the enzyme. In this work, genetic, biophysical and structural approaches were taken to dissect the interaction between NapD and the NapA signal peptide. A NapD binding epitope was identified towards the N-terminus of the signal peptide, which overlapped significantly with the twin-arginine targeting motif. NMR spectroscopy revealed that the signal peptide adopted a a-helical conformation when bound by NapD, and substitution of single residues within the NapA signal peptide was sufficient to disrupt the interaction. This work provides an increased level of understanding of signal peptide function on the bacterial Tat pathway.</p>

AB - <p>The twin-arginine translocation (Tat) pathway is a protein targeting system present in many prokaryotes. The physiological role of the Tat pathway is the transmembrane translocation of fully-folded proteins, which are targeted by N-terminal signal peptides bearing conserved SRRxFLK twin-arginine amino acid motifs. In Escherichia coli the majority of Tat targeted proteins bind redox cofactors and it is important that only mature, cofactor-loaded precursors are presented for export. Cellular processes have been unearthed that sequence these events, for example the signal peptide of the periplasmic nitrate reductase (NapA) is bound by a cytoplasmic chaperone (NapD) that is thought to regulate assembly and export of the enzyme. In this work, genetic, biophysical and structural approaches were taken to dissect the interaction between NapD and the NapA signal peptide. A NapD binding epitope was identified towards the N-terminus of the signal peptide, which overlapped significantly with the twin-arginine targeting motif. NMR spectroscopy revealed that the signal peptide adopted a a-helical conformation when bound by NapD, and substitution of single residues within the NapA signal peptide was sufficient to disrupt the interaction. This work provides an increased level of understanding of signal peptide function on the bacterial Tat pathway.</p>

U2 - 10.1111/j.1365-2958.2012.08005.x

DO - 10.1111/j.1365-2958.2012.08005.x

M1 - Article

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 6

VL - 83

SP - 1254

EP - 1267

ER -

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